FLI1_HUMAN
ID FLI1_HUMAN Reviewed; 452 AA.
AC Q01543; B2R8H2; B4DFV4; B4DTC6; G3V183; Q14319; Q92480; Q9UE07;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Friend leukemia integration 1 transcription factor;
DE AltName: Full=Proto-oncogene Fli-1;
DE AltName: Full=Transcription factor ERGB;
GN Name=FLI1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Bone marrow;
RX PubMed=1522903; DOI=10.1038/359162a0;
RA Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M.,
RA Kovar H., Joubert I., de Jong P., Rouleau G., Aurias A., Thomas G.;
RT "Gene fusion with an ETS DNA-binding domain caused by chromosome
RT translocation in human tumours.";
RL Nature 359:162-165(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1445800;
RA Watson D.K., Smyth F.E., Thompson D.M., Cheng J.Q., Testa J.R., Papas T.S.,
RA Seth A.;
RT "The ERGB/Fli-1 gene: isolation and characterization of a new member of the
RT family of human ETS transcription factors.";
RL Cell Growth Differ. 3:705-713(1992).
RN [3]
RP SEQUENCE REVISION.
RA Watson D.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1394211;
RA Prasad D.D., Rao V.N., Reddy E.S.;
RT "Structure and expression of human Fli-1 gene.";
RL Cancer Res. 52:5833-5837(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood;
RX PubMed=8439553; DOI=10.1016/0167-4781(93)90283-j;
RA Hromas R., May W., Denny C., Raskind W., Moore J., Maki R.A., Beck E.,
RA Klemsz M.J.;
RT "Human FLI-1 localizes to chromosome 11q24 and has an aberrant transcript
RT in neuroepithelioma.";
RL Biochim. Biophys. Acta 1172:155-158(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHROMOSOMAL
RP TRANSLOCATION.
RX PubMed=1765382; DOI=10.1016/0888-7543(91)90124-w;
RA Baud V., Lipinski M., Rassart E., Poliquin L., Bergeron D.;
RT "The human homolog of the mouse common viral integration region, FLI1, maps
RT to 11q23-q24.";
RL Genomics 11:223-224(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ubhi B.T.S., Rainey D.R., Meredith D.M.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Amygdala, Placenta, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-452.
RX PubMed=9751743; DOI=10.1073/pnas.95.20.11786;
RA Zucman-Rossi J., Legoix P., Victor J.M., Lopez B., Thomas G.;
RT "Chromosome translocation based on illegitimate recombination in human
RT tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11786-11791(1998).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-301.
RC TISSUE=Placenta;
RX PubMed=7542907; DOI=10.1002/gcc.2870130209;
RA Bhagirath T., Abe S., Nojima T., Yoshida M.C.;
RT "Molecular analysis of a t(11;22) translocation junction in a case of
RT Ewing's sarcoma.";
RL Genes Chromosomes Cancer 13:126-132(1995).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21 TRP-337 AND CYS-343, AND
RP CHARACTERIZATION OF VARIANTS BDPLT21 TRP-337 AND CYS-343.
RX PubMed=24100448; DOI=10.1182/blood-2013-06-506873;
RG UK Genotyping and Phenotyping of Platelets Study Group;
RA Stockley J., Morgan N.V., Bem D., Lowe G.C., Lordkipanidze M., Dawood B.,
RA Simpson M.A., Macfarlane K., Horner K., Leo V.C., Talks K., Motwani J.,
RA Wilde J.T., Collins P.W., Makris M., Watson S.P., Daly M.E.;
RT "Enrichment of FLI1 and RUNX1 mutations in families with excessive bleeding
RT and platelet dense granule secretion defects.";
RL Blood 122:4090-4093(2013).
RN [16]
RP FUNCTION, INVOLVEMENT IN BDPLT21, VARIANT BDPLT21 TRP-324, AND
RP CHARACTERIZATION OF VARIANT BDPLT21 TRP-324.
RX PubMed=26316623; DOI=10.1182/blood-2015-06-650887;
RA Stevenson W.S., Rabbolini D.J., Beutler L., Chen Q., Gabrielli S.,
RA Mackay J.P., Brighton T.A., Ward C.M., Morel-Kopp M.C.;
RT "Paris-Trousseau thrombocytopenia is phenocopied by the autosomal recessive
RT inheritance of a DNA-binding domain mutation in FLI1.";
RL Blood 126:2027-2030(2015).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21
RP GLN-337 AND GLU-345, AND CHARACTERIZATION OF VARIANTS BDPLT21 GLN-337 AND
RP GLU-345.
RX PubMed=28255014; DOI=10.3324/haematol.2016.153577;
RA Saultier P., Vidal L., Canault M., Bernot D., Falaise C., Pouymayou C.,
RA Bordet J.C., Saut N., Rostan A., Baccini V., Peiretti F., Favier M.,
RA Lucca P., Deleuze J.F., Olaso R., Boland A., Morange P.E., Gachet C.,
RA Malergue F., Faure S., Eckly A., Tregouet D.A., Poggi M., Alessi M.C.;
RT "Macrothrombocytopenia and dense granule deficiency associated with FLI1
RT variants: ultrastructural and pathogenic features.";
RL Haematologica 102:1006-1016(2017).
RN [18]
RP STRUCTURE BY NMR OF 276-373.
RX PubMed=7773776; DOI=10.1038/nsb1294-871;
RA Liang H., Mao X., Olejniczak E.T., Nettesheim D.G., Yu L., Meadows R.P.,
RA Thompson C.B., Fesik S.W.;
RT "Solution structure of the ets domain of Fli-1 when bound to DNA.";
RL Nat. Struct. Biol. 1:871-875(1994).
RN [19]
RP STRUCTURE BY NMR OF 114-198.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAM_pnt-domain of the human Friend leukemia
RT integration 1 transcription factor.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Sequence-specific transcriptional activator (PubMed:24100448,
CC PubMed:26316623, PubMed:28255014). Recognizes the DNA sequence 5'-
CC C[CA]GGAAGT-3'. {ECO:0000269|PubMed:24100448,
CC ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}.
CC -!- SUBUNIT: Can form homodimers or heterodimers with ETV6/TEL1.
CC -!- INTERACTION:
CC Q01543; P56545-3: CTBP2; NbExp=3; IntAct=EBI-2271018, EBI-10171902;
CC Q01543; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2271018, EBI-747107;
CC Q01543; P84022: SMAD3; NbExp=3; IntAct=EBI-2271018, EBI-347161;
CC Q01543; O94993: SOX30; NbExp=3; IntAct=EBI-2271018, EBI-742973;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28255014}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q01543-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01543-2; Sequence=VSP_001478;
CC Name=3;
CC IsoId=Q01543-3; Sequence=VSP_045276;
CC Name=4;
CC IsoId=Q01543-4; Sequence=VSP_046943;
CC -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC metastatic, primitive small round cell tumor of bone and soft tissue
CC that affects children and adolescents. It belongs to the Ewing sarcoma
CC family of tumors, a group of morphologically heterogeneous neoplasms
CC that share the same cytogenetic features. They are considered neural
CC tumors derived from cells of the neural crest. Ewing sarcoma represents
CC the less differentiated form of the tumors.
CC {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}. Note=The gene
CC represented in this entry is involved in disease pathogenesis. A
CC chromosomal aberration involving FLI1 is found in patients with Erwing
CC sarcoma. Translocation t(11;22)(q24;q12) with EWSR1.
CC {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}.
CC -!- DISEASE: Bleeding disorder, platelet-type, 21 (BDPLT21) [MIM:617443]: A
CC disorder characterized by increased bleeding tendency due to platelet
CC dysfunction. Clinical features include epistaxis, hematomas, bleeding
CC after tooth extraction, and menorrhagia. BDPLT21 patients may have mild
CC to moderate thrombocytopenia. {ECO:0000269|PubMed:24100448,
CC ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Located on a fragment of chromosome 11 flanked on the
CC centromeric side by the acute lymphoblastic leukemia-associated
CC t(4;11)(q21;q23) translocation breakpoint and on the telomeric side by
CC the Ewing- and neuroepithelioma-associated t(11;22) (q24;q12)
CC breakpoint.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FLI1ID79ch11q24.html";
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DR EMBL; X67001; CAA47399.1; -; mRNA.
DR EMBL; M98833; AAA35812.2; -; mRNA.
DR EMBL; S45205; AAB23637.1; -; mRNA.
DR EMBL; M93255; AAA58479.1; -; mRNA.
DR EMBL; M93255; AAA58480.1; -; mRNA.
DR EMBL; AY029368; AAK50443.1; -; mRNA.
DR EMBL; AK294279; BAG57565.1; -; mRNA.
DR EMBL; AK300153; BAG61938.1; -; mRNA.
DR EMBL; AK313370; BAG36169.1; -; mRNA.
DR EMBL; AP001122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67715.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67718.1; -; Genomic_DNA.
DR EMBL; BC001670; AAH01670.1; -; mRNA.
DR EMBL; BC010115; AAH10115.1; -; mRNA.
DR EMBL; Y17293; CAA76731.1; -; Genomic_DNA.
DR EMBL; D38408; BAA07463.1; ALT_TERM; Genomic_DNA.
DR CCDS; CCDS44768.1; -. [Q01543-1]
DR CCDS; CCDS53725.1; -. [Q01543-3]
DR CCDS; CCDS59230.1; -. [Q01543-4]
DR CCDS; CCDS59231.1; -. [Q01543-2]
DR PIR; I37565; I37565.
DR PIR; S29844; S29844.
DR RefSeq; NP_001161153.1; NM_001167681.2. [Q01543-3]
DR RefSeq; NP_001257939.1; NM_001271010.1. [Q01543-2]
DR RefSeq; NP_001257941.1; NM_001271012.1. [Q01543-4]
DR RefSeq; NP_002008.2; NM_002017.4. [Q01543-1]
DR RefSeq; XP_011541003.1; XM_011542701.2. [Q01543-3]
DR RefSeq; XP_016872894.1; XM_017017405.1. [Q01543-3]
DR RefSeq; XP_016872895.1; XM_017017406.1. [Q01543-3]
DR PDB; 1FLI; NMR; -; A=276-373.
DR PDB; 1X66; NMR; -; A=114-198.
DR PDB; 2YTU; NMR; -; A=100-220.
DR PDB; 5E8G; X-ray; 2.70 A; A/B/C/D=276-399.
DR PDB; 5E8I; X-ray; 3.45 A; A/D/G/J=276-399.
DR PDB; 5JVT; X-ray; 3.10 A; A/D/G=276-375.
DR PDB; 6VG2; X-ray; 3.90 A; A/D=276-375.
DR PDB; 6VG8; X-ray; 4.31 A; A=276-375.
DR PDB; 6VGD; X-ray; 4.20 A; A=276-375.
DR PDBsum; 1FLI; -.
DR PDBsum; 1X66; -.
DR PDBsum; 2YTU; -.
DR PDBsum; 5E8G; -.
DR PDBsum; 5E8I; -.
DR PDBsum; 5JVT; -.
DR PDBsum; 6VG2; -.
DR PDBsum; 6VG8; -.
DR PDBsum; 6VGD; -.
DR AlphaFoldDB; Q01543; -.
DR BMRB; Q01543; -.
DR SMR; Q01543; -.
DR BioGRID; 108602; 46.
DR CORUM; Q01543; -.
DR IntAct; Q01543; 16.
DR MINT; Q01543; -.
DR STRING; 9606.ENSP00000433488; -.
DR BindingDB; Q01543; -.
DR GlyGen; Q01543; 14 sites, 2 O-linked glycans (14 sites).
DR iPTMnet; Q01543; -.
DR MetOSite; Q01543; -.
DR PhosphoSitePlus; Q01543; -.
DR BioMuta; FLI1; -.
DR DMDM; 399496; -.
DR EPD; Q01543; -.
DR jPOST; Q01543; -.
DR MassIVE; Q01543; -.
DR MaxQB; Q01543; -.
DR PaxDb; Q01543; -.
DR PeptideAtlas; Q01543; -.
DR PRIDE; Q01543; -.
DR ProteomicsDB; 32288; -.
DR ProteomicsDB; 4083; -.
DR ProteomicsDB; 57969; -. [Q01543-1]
DR ProteomicsDB; 57970; -. [Q01543-2]
DR Antibodypedia; 9350; 698 antibodies from 43 providers.
DR DNASU; 2313; -.
DR Ensembl; ENST00000281428.12; ENSP00000281428.8; ENSG00000151702.17. [Q01543-2]
DR Ensembl; ENST00000344954.10; ENSP00000339627.7; ENSG00000151702.17. [Q01543-4]
DR Ensembl; ENST00000527786.7; ENSP00000433488.2; ENSG00000151702.17. [Q01543-1]
DR Ensembl; ENST00000534087.3; ENSP00000432950.1; ENSG00000151702.17. [Q01543-3]
DR GeneID; 2313; -.
DR KEGG; hsa:2313; -.
DR MANE-Select; ENST00000527786.7; ENSP00000433488.2; NM_002017.5; NP_002008.2.
DR UCSC; uc009zci.4; human. [Q01543-1]
DR CTD; 2313; -.
DR DisGeNET; 2313; -.
DR GeneCards; FLI1; -.
DR HGNC; HGNC:3749; FLI1.
DR HPA; ENSG00000151702; Tissue enhanced (lymphoid).
DR MalaCards; FLI1; -.
DR MIM; 193067; gene.
DR MIM; 612219; phenotype.
DR MIM; 617443; phenotype.
DR neXtProt; NX_Q01543; -.
DR OpenTargets; ENSG00000151702; -.
DR Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR Orphanet; 248340; Isolated delta-storage pool disease.
DR Orphanet; 2308; Jacobsen syndrome.
DR Orphanet; 851; Paris-Trousseau thrombocytopenia.
DR Orphanet; 370348; Peripheral primitive neuroectodermal tumor.
DR Orphanet; 319; Skeletal Ewing sarcoma.
DR PharmGKB; PA28170; -.
DR VEuPathDB; HostDB:ENSG00000151702; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000158261; -.
DR HOGENOM; CLU_933700_0_0_1; -.
DR InParanoid; Q01543; -.
DR OMA; XSLLAYN; -.
DR PhylomeDB; Q01543; -.
DR TreeFam; TF350537; -.
DR PathwayCommons; Q01543; -.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q01543; -.
DR SIGNOR; Q01543; -.
DR BioGRID-ORCS; 2313; 59 hits in 1100 CRISPR screens.
DR ChiTaRS; FLI1; human.
DR EvolutionaryTrace; Q01543; -.
DR GeneWiki; FLI1; -.
DR GenomeRNAi; 2313; -.
DR Pharos; Q01543; Tbio.
DR PRO; PR:Q01543; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q01543; protein.
DR Bgee; ENSG00000151702; Expressed in monocyte and 166 other tissues.
DR ExpressionAtlas; Q01543; baseline and differential.
DR Genevisible; Q01543; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007599; P:hemostasis; TAS:ProtInc.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd08541; SAM_PNT-FLI-1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR035575; Fli-1.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR035573; SAM_PNT-FLI-1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF161; PTHR11849:SF161; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement;
KW Disease variant; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..452
FT /note="Friend leukemia integration 1 transcription factor"
FT /id="PRO_0000204124"
FT DOMAIN 112..198
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 281..361
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 209..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26323"
FT VAR_SEQ 1..197
FT /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP
FT PQQEWINQPVRVNVKREYDHMNGSRESPVDCSVSKCSKLVGGGESNPMNYNSYMDEKNG
FT PPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYSLMEIDTSFFQNMDGKELCKM
FT NKEDFLRATTLYNTEVLLSHLSYLRES -> MDPG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046943"
FT VAR_SEQ 1..76
FT /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP
FT PQQEWINQPVRVNVKREYDHMNGS -> MEGGLAGERA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1765382,
FT ECO:0000303|PubMed:8439553"
FT /id="VSP_001478"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045276"
FT VARIANT 324
FT /note="R -> W (in BDPLT21; decreased function in positive
FT regulation of DNA-templated transcription;
FT dbSNP:rs773148506)"
FT /evidence="ECO:0000269|PubMed:26316623"
FT /id="VAR_078929"
FT VARIANT 337
FT /note="R -> Q (in BDPLT21; loss of function in positive
FT regulation of DNA-templated transcription; decreased
FT localization to nucleus; no effect on protein abundance;
FT dbSNP:rs1064797086)"
FT /evidence="ECO:0000269|PubMed:28255014"
FT /id="VAR_078930"
FT VARIANT 337
FT /note="R -> W (in BDPLT21; loss of function in positive
FT regulation of DNA-templated transcription;
FT dbSNP:rs1064797083)"
FT /evidence="ECO:0000269|PubMed:24100448"
FT /id="VAR_078931"
FT VARIANT 343
FT /note="Y -> C (in BDPLT21; loss of function in positive
FT regulation of DNA-templated transcription;
FT dbSNP:rs1064797084)"
FT /evidence="ECO:0000269|PubMed:24100448"
FT /id="VAR_078932"
FT VARIANT 345
FT /note="K -> E (in BDPLT21; loss of function in positive
FT regulation of DNA-templated transcription; decreased
FT localization to nucleus; no effect on protein abundance;
FT dbSNP:rs1064797087)"
FT /evidence="ECO:0000269|PubMed:28255014"
FT /id="VAR_078933"
FT CONFLICT 69
FT /note="E -> V (in Ref. 5; AAA58479)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Missing (in Ref. 5; AAA58479)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="P -> A (in Ref. 5; AAA58479/AAA58480)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="W -> V (in Ref. 5; AAA58479/AAA58480)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> N (in Ref. 8; BAG61938)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="E -> Q (in Ref. 4; AAB23637 and 5; AAA58479/
FT AAA58480)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="Missing (in Ref. 5; AAA58479/AAA58480)"
FT /evidence="ECO:0000305"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2YTU"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:1X66"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:5E8G"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5E8G"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5E8G"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5E8I"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5E8G"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:5E8G"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:5E8G"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5E8G"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:5E8G"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:5E8G"
SQ SEQUENCE 452 AA; 50982 MW; 9C2AAEEAF683F3FA CRC64;
MDGTIKEALS VVSDDQSLFD SAYGAAAHLP KADMTASGSP DYGQPHKINP LPPQQEWINQ
PVRVNVKREY DHMNGSRESP VDCSVSKCSK LVGGGESNPM NYNSYMDEKN GPPPPNMTTN
ERRVIVPADP TLWTQEHVRQ WLEWAIKEYS LMEIDTSFFQ NMDGKELCKM NKEDFLRATT
LYNTEVLLSH LSYLRESSLL AYNTTSHTDQ SSRLSVKEDP SYDSVRRGAW GNNMNSGLNK
SPPLGGAQTI SKNTEQRPQP DPYQILGPTS SRLANPGSGQ IQLWQFLLEL LSDSANASCI
TWEGTNGEFK MTDPDEVARR WGERKSKPNM NYDKLSRALR YYYDKNIMTK VHGKRYAYKF
DFHGIAQALQ PHPTESSMYK YPSDISYMPS YHAHQQKVNF VPPHPSSMPV TSSSFFGAAS
QYWTSPTGGI YPNPNVPRHP NTHVPSHLGS YY
